On the basis of enzymic properties, different fibre types can be distinguished in human skeletal muscle (type I fibres and type II fibres with subtypes) and there is a correlation between fibre types and the occurrence of slow and fast myosin. In human masticatory muscles, fibres with ATPase activity at pH 9.4, intermediate between that of type I (low activity) and type II (high activity), are frequent. On cryostat-sectioned material, highly specific antibodies against fast myosin, slow myosin and slow light chains were applied. The myosin composition of human masticatory muscles was very heterogeneous, in contrast to that in limb muscles, with various proportions of slow and fast myosins, heavy as well as light chains. Type I fibres contained slow myosin only and type II mainly fast myosin, ATPase IM and type IIC fibres contained a mixture of slow and fast myosins in variable amounts. The findings conform with physiological evidence of a continuum of contraction times for motor units in the human masticatory muscles and suggests that these muscles are highly adapted to the special and complicated functions of the stomatognathic system.